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Volumn 1770, Issue 9, 2007, Pages 1374-1381

Engineering the enantioselectivity of glutathione transferase by combined active-site mutations and chemical modifications

Author keywords

Enantioselectivity; Epoxide resolution; Glutathione transferase; Protein modification; Rational redesign

Indexed keywords

CYSTEINE; EPOXIDE; GLUTATHIONE TRANSFERASE; RECOMBINANT ENZYME;

EID: 34547844239     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.06.002     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 0035471137 scopus 로고    scopus 로고
    • Generation of new enzymes via covalent modifications of existing proteins
    • Qi D., Tann C.-M., Haring D., and Distefano D. Generation of new enzymes via covalent modifications of existing proteins. Chem. Rev. 101 (2001) 3081-3112
    • (2001) Chem. Rev. , vol.101 , pp. 3081-3112
    • Qi, D.1    Tann, C.-M.2    Haring, D.3    Distefano, D.4
  • 2
    • 0032574793 scopus 로고    scopus 로고
    • Site-directed mutagenesis combined with chemical modifications as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus
    • DeSantis G., Berglund P., Stabile M.R., Gold M., and Jones J.B. Site-directed mutagenesis combined with chemical modifications as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus. Biochemistry 37 (1998) 5968-5973
    • (1998) Biochemistry , vol.37 , pp. 5968-5973
    • DeSantis, G.1    Berglund, P.2    Stabile, M.R.3    Gold, M.4    Jones, J.B.5
  • 3
    • 0032589512 scopus 로고    scopus 로고
    • Chemical modifications of enzymes for enhanced functionality
    • DeSantis G., Shang X., and Jones J.B. Chemical modifications of enzymes for enhanced functionality. Biochemistry 38 (1999) 13391-13397
    • (1999) Biochemistry , vol.38 , pp. 13391-13397
    • DeSantis, G.1    Shang, X.2    Jones, J.B.3
  • 4
    • 0023928933 scopus 로고
    • Stereoselectivity and regioselectivity of purified human glutathione transferases pi, alpha-epsilon, and mu with alkene and polycyclic arene oxide substrates
    • Dostal L.A., Guthenberg C., Mannervik B., and Bend J.R. Stereoselectivity and regioselectivity of purified human glutathione transferases pi, alpha-epsilon, and mu with alkene and polycyclic arene oxide substrates. Drug Metab. Dispos. 16 (1988) 420-424
    • (1988) Drug Metab. Dispos. , vol.16 , pp. 420-424
    • Dostal, L.A.1    Guthenberg, C.2    Mannervik, B.3    Bend, J.R.4
  • 5
    • 27944441021 scopus 로고    scopus 로고
    • Regio- and enantioselectivity in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases
    • Ivarsson Y., and Mannervik B. Regio- and enantioselectivity in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases. Protein Eng. Des. Sel. 18 (2005) 607-616
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 607-616
    • Ivarsson, Y.1    Mannervik, B.2
  • 6
    • 0030822939 scopus 로고    scopus 로고
    • Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1
    • Sundberg K., Widersten M., Seidel A., Mannervik B., and Jernström B. Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1. Chem. Res. Toxicol. 10 (1997) 1221-1227
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1221-1227
    • Sundberg, K.1    Widersten, M.2    Seidel, A.3    Mannervik, B.4    Jernström, B.5
  • 7
    • 0030869888 scopus 로고    scopus 로고
    • Epoxide hydrolases as asymmetric catalysts
    • Archer I.V.J. Epoxide hydrolases as asymmetric catalysts. Tetrahedron 53 (1997) 15617-15662
    • (1997) Tetrahedron , vol.53 , pp. 15617-15662
    • Archer, I.V.J.1
  • 8
    • 0035313421 scopus 로고    scopus 로고
    • Synthetic applications of epoxide hydrolases
    • Archelas A., and Furstos R. Synthetic applications of epoxide hydrolases. Curr. Opin. Chem. Biol. 5 (2001) 112-119
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 112-119
    • Archelas, A.1    Furstos, R.2
  • 10
    • 0025999878 scopus 로고
    • Cysteine residues are not essential for the catalytic activity of human Mu class glutathione transferase M1a-1a
    • Widersten M., Holmström E., and Mannervik B. Cysteine residues are not essential for the catalytic activity of human Mu class glutathione transferase M1a-1a. FEBS Lett. 293 (1991) 156-159
    • (1991) FEBS Lett. , vol.293 , pp. 156-159
    • Widersten, M.1    Holmström, E.2    Mannervik, B.3
  • 11
    • 0028605708 scopus 로고
    • Rational reconstruction of the active site of a class mu glutathione S-transferase
    • Shan S., and Armstrong R.N. Rational reconstruction of the active site of a class mu glutathione S-transferase. J. Biol. Chem. 269 (1994) 32373-32379
    • (1994) J. Biol. Chem. , vol.269 , pp. 32373-32379
    • Shan, S.1    Armstrong, R.N.2
  • 12
    • 0026513368 scopus 로고
    • Design of two chimaeric human-rat class Alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties
    • Björnestedt R., Widersten M., Board P.G., and Mannervik B. Design of two chimaeric human-rat class Alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties. Biochem. J. 282 (1992) 505-510
    • (1992) Biochem. J. , vol.282 , pp. 505-510
    • Björnestedt, R.1    Widersten, M.2    Board, P.G.3    Mannervik, B.4
  • 13
    • 0030175041 scopus 로고    scopus 로고
    • Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA
    • Widersten M., Huang M., and Mannervik B. Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA. Protein Expr. Purif. 7 (1996) 367-372
    • (1996) Protein Expr. Purif. , vol.7 , pp. 367-372
    • Widersten, M.1    Huang, M.2    Mannervik, B.3
  • 14
    • 0037424257 scopus 로고    scopus 로고
    • Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign
    • Ivarsson Y., Mackey A.J., Edalat M., Pearson R., and Mannervik B. Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign. J. Biol. Chem. 278 (2003) 8733-8738
    • (2003) J. Biol. Chem. , vol.278 , pp. 8733-8738
    • Ivarsson, Y.1    Mackey, A.J.2    Edalat, M.3    Pearson, R.4    Mannervik, B.5
  • 15
    • 0033212786 scopus 로고    scopus 로고
    • Use of silent mutations in cDNA encoding human glutathione transferase M2-2 for optimized expression in Escherichia coli
    • Johansson A.-S., Bolton-Grob R., and Mannervik B. Use of silent mutations in cDNA encoding human glutathione transferase M2-2 for optimized expression in Escherichia coli. Protein Expr. Purif. 17 (1999) 105-112
    • (1999) Protein Expr. Purif. , vol.17 , pp. 105-112
    • Johansson, A.-S.1    Bolton-Grob, R.2    Mannervik, B.3
  • 16
    • 33748554496 scopus 로고    scopus 로고
    • Replacement surgery with unnatural amino acids in the lock-and-key joint of glutathione transferase subunits
    • Hegazy U.M., and Mannervik B. Replacement surgery with unnatural amino acids in the lock-and-key joint of glutathione transferase subunits. Chem. Biol. 13 (2006) 929-936
    • (2006) Chem. Biol. , vol.13 , pp. 929-936
    • Hegazy, U.M.1    Mannervik, B.2
  • 18
    • 0036383921 scopus 로고    scopus 로고
    • Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector
    • Hellman U., and Bhikhabhai R. Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. Rapid Commun. Mass Spectrom. 16 (2002) 1851-1859
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1851-1859
    • Hellman, U.1    Bhikhabhai, R.2
  • 19
    • 33645529663 scopus 로고    scopus 로고
    • Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution
    • Norrgård M.A., Ivarsson Y., Tars K., and Mannervik B. Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4876-4881
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4876-4881
    • Norrgård, M.A.1    Ivarsson, Y.2    Tars, K.3    Mannervik, B.4
  • 21
    • 0142091405 scopus 로고    scopus 로고
    • The near attack conformation approach to the study of the chorismate to prephenate reaction
    • Hur S., and Bruice T.C. The near attack conformation approach to the study of the chorismate to prephenate reaction. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 12015-12020
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12015-12020
    • Hur, S.1    Bruice, T.C.2
  • 22
    • 27744485401 scopus 로고    scopus 로고
    • Adding amino acids to the genetic repertoire
    • Xie J., and Schultz P.G. Adding amino acids to the genetic repertoire. Curr. Opin. Chem. Biol. 9 (2005) 548-554
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 548-554
    • Xie, J.1    Schultz, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.